Mitochondrial uncoupling and lifespan

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How mitochondria produce reactive oxygen species

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Identification and Importance of Brown Adipose Tissue in Adult Humans

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Cold-Activated Brown Adipose Tissue in Healthy Men

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A C. elegans mutant that lives twice as long as wild type

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Functional Brown Adipose Tissue in Healthy Adults

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High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria

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Extension of murine life span by overexpression of catalase targeted to mitochondria

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Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia

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Superoxide activates mitochondrial uncoupling proteins

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Mitochondrial metabolism of reactive oxygen species

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UCP1 Ablation Induces Obesity and Abolishes Diet-Induced Thermogenesis in Mice Exempt from Thermal Stress by Living at Thermoneutrality

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Mitochondria and reactive oxygen species

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Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production

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Electron transfer by domain movement in cytochrome bc1

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Uncoupling protein‐3: a new member of the mitochondrial carrier family with tissue‐specific expression

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Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins

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Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, β-cell dysfunction, and type 2 diabetes.

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The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP

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Uncoupling to survive? The role of mitochondrial inefficiency in ageing

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Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3

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The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains

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Uncoupled and surviving: individual mice with high metabolism have greater mitochondrial uncoupling and live longer

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Uncoupling Protein-3 Is a Mediator of Thermogenesis Regulated by Thyroid Hormone, β3-Adrenergic Agonists, and Leptin

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The presence of UCP1 demonstrates that metabolically active adipose tissue in the neck of adult humans truly represents brown adipose tissue

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The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria

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Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells

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UCP3: An Uncoupling Protein Homologue Expressed Preferentially and Abundantly in Skeletal Muscle and Brown Adipose Tissue

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Energy metabolism in uncoupling protein 3 gene knockout mice

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The Rate of Living.

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The mitochondrial uncoupling-protein homologues

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Increased dosage of mammalian Sir2 in pancreatic β cells enhances glucose-stimulated insulin secretion in mice

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The ADP and ATP transport in mitochondria and its carrier

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Mice overexpressing human uncoupling protein-3 in skeletal muscle are hyperphagic and lean

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Is the oxidative stress theory of aging dead?

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A signalling role for 4‐hydroxy‐2‐nonenal in regulation of mitochondrial uncoupling

Echtay, K. S., Esteves, T. C., Pakay, J. L., Jekabsons, M. B., Lambert, A. J., Portero‐Otín, M., Pamplona, R., Vidal‐Puig, A. J., Wang, S., Roebuck, S. J., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg412 · Cited by 597 · see citing works

Reactive Oxygen Species as a Signal in Glucose-Stimulated Insulin Secretion

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Insulin resistance is a cellular antioxidant defense mechanism

Hoehn, K. L., Salmon, A. B., Hohnen-Behrens, C., Turner, N., Hoy, A. J., Maghzal, G. J., Stocker, R., Van Remmen, H., Kraegen, E. W., Cooney, G. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902380106 · Cited by 540 · see citing works

Demography of Dietary Restriction and Death in Drosophila

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Only UCP1 can mediate adaptive nonshivering thermogenesis in the cold

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Overexpression of Catalase Targeted to Mitochondria Attenuates Murine Cardiac Aging

Dai, D., Santana, L. F., Vermulst, M., Tomazela, D. M., Emond, M. J., MacCoss, M. J., Gollahon, K. A., Martin, G. M., Loeb, L. A., Ladiges, W., et al. (2009) · Circulation · doi:10.1161/circulationaha.108.822403 · Cited by 497 · see citing works

Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial nadh:Ubiquinone oxidoreductase (complex i)

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Uncoupling Protein 2, in Vivo Distribution, Induction upon Oxidative Stress, and Evidence for Translational Regulation

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Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane

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The causes and functions of mitochondrial proton leak

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Reactive oxygen species, mitochondria, apoptosis and aging

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Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction

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Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction

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Transgenic Mice with a Reduced Core Body Temperature Have an Increased Life Span

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Reactive oxygen species, mitochondria, apoptosis and aging

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Superoxide Activates Mitochondrial Uncoupling Protein 2 from the Matrix Side

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UCP4, a novel brain‐specific mitochondrial protein that reduces membrane potential in mammalian cells

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Reactive Oxygen Species Production by Mitochondria

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Mild mitochondrial uncoupling in mice affects energy metabolism, redox balance and longevity

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Basic aspects of the biochemical reactivity of 4-hydroxynonenal

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Mitochondrial uncoupling proteins—What is their physiological role?

Echtay, K. S. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.011 · Cited by 338 · see citing works

Age-related hearing loss in C57BL/6J mice is mediated by Bak-dependent mitochondrial apoptosis

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Physiological Role of UCP3 May Be Export of Fatty Acids from Mitochondria When Fatty Acid Oxidation Predominates: An Hypothesis

Himms‐Hagen, J., & Harper, M. (2001) · Experimental Biology and Medicine · doi:10.1177/153537020122600204 · Cited by 325 · see citing works

BMCP1, a Novel Mitochondrial Carrier with High Expression in the Central Nervous System of Humans and Rodents, and Respiration Uncoupling Activity in Recombinant Yeast

Sanchı́s, D., Fleury, C., Chomiki, N., Goubern, M., Huang, Q., Neverova, M., Gregoire, F. M., Easlick, J. L., Raimbault, S., Lévi-Meyrueis, C., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.34611 · Cited by 310 · see citing works

Superoxide Activates Uncoupling Proteins by Generating Carbon-centered Radicals and Initiating Lipid Peroxidation

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Skeletal muscle respiratory uncoupling prevents diet-induced obesity and insulin resistance in mice

Li, B., Nolte, L. A., Ju, J.-S., Ho Han, D., Coleman, T., Holloszy, J. O., & Semenkovich, C. F. (2000) · Nature Medicine · doi:10.1038/80450 · Cited by 291 · see citing works

Increased superoxide in vivo accelerates age‐associated muscle atrophy through mitochondrial dysfunction and neuromuscular junction degeneration

Jang, Y. C., Lustgarten, M. S., Liu, Y., Müller, F. L., Bhattacharya, A., Liang, H., Salmon, A. B., Brooks, S. V., Larkin, L. M., Hayworth, C. R., et al. (2009) · The FASEB Journal · doi:10.1096/fj.09-146308 · Cited by 290 · see citing works

Mitochondrial matrix reactive oxygen species production is very sensitive to mild uncoupling

Miwa, S., & Brand, M. D. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311300 · Cited by 288 · see citing works

Low rates of hydrogen peroxide production by isolated heart mitochondria associate with long maximum lifespan in vertebrate homeotherms

Lambert, A. J., Boysen, H. M., Buckingham, J. A., Yang, T., Podlutsky, A. J., Austad, S. N., Kunz, T., Buffenstein, R., & Brand, M. D. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00312.x · Cited by 264 · see citing works

Mitochondrial uncoupling as a target for drug development for the treatment of obesity.

Harper, J. A., Dickinson, K., & Brand, M. D. (2001) · Obesity Reviews · doi:10.1046/j.1467-789x.2001.00043.x · Cited by 250 · see citing works

4-Hydroxynonenal As a Biological Signal: Molecular Basis and Pathophysiological Implications

Parola, M., Bellomo, G., Robino, G., Barrera, G., & Dianzani, M. U. (1999) · Antioxidants and Redox Signaling · doi:10.1089/ars.1999.1.3-255 · Cited by 250 · see citing works

Mitochondrial Free Radical Production and Aging in Mammals and Birdsa

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Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets.

Chan, C. B., MacDonald, P. E., Saleh, M. C., Johns, D. C., Marbàn, E., & Wheeler, M. B. (1999) · Diabetes · doi:10.2337/diabetes.48.7.1482 · Cited by 242 · see citing works

Protective Role of Uncoupling Protein 2 in Atherosclerosis

Blanc, J., Alves‐Guerra, M., Esposito, B., Rousset, S., Gourdy, P., Ricquier, D., Tedgui, A., Miroux, B., & Mallat, Z. (2003) · Circulation · doi:10.1161/01.cir.0000051722.66074.60 · Cited by 239 · see citing works

UCP2 and UCP3 rise in starved rat skeletal muscle but mitochondrial proton conductance is unchanged

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Uncoupling Protein 2: A Possible Link Between Fatty Acid Excess and Impaired Glucose-Induced Insulin Secretion?

Davis‐Lameloise, N., Muzzin, P., Prentki, M., & Assimacopoulos‐Jeannet, F. (2001) · Diabetes · doi:10.2337/diabetes.50.4.803 · Cited by 226 · see citing works

Mild mitochondrial uncoupling impacts cellular aging in human muscles in vivo

Amara, C. E., Shankland, E. G., Jubrias, S. A., Marcinek, D. J., Kushmerick, M. J., & Conley, K. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610131104 · Cited by 223 · see citing works

Tissue‐dependent upregulation of rat uncoupling protein‐2 expression in response to fasting or cold

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Generating, Partitioning, Targeting and Functioning of Superoxide in Mitochondria

Liu, S. (1997) · Bioscience Reports · doi:10.1023/a:1027328510931 · Cited by 217 · see citing works

UCP1 deficiency increases susceptibility to diet‐induced obesity with age

Kontani, Y., Wang, Y., Kimura, K., Inokuma, K. ‐., Saito, M., Suzuki‐Miura, T., Wang, Z., Sato, Y., Mori, N., & Yamashita, H. (2005) · Aging Cell · doi:10.1111/j.1474-9726.2005.00157.x · Cited by 207 · see citing works

Free Fatty Acid-induced β-Cell Defects Are Dependent on Uncoupling Protein 2 Expression

Joseph, J. W., Koshkin, V., Saleh, M. C., Sivitz, W. I., Zhang, C.-Y., Lowell, B. B., Chan, C. B., & Wheeler, M. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409189200 · Cited by 206 · see citing works

Overexpression of Mn Superoxide Dismutase Does Not Increase Life Span in Mice

Jang, Y. C., Pérez, V., Song, W. J., Lustgarten, M. S., Salmon, A. B., Mele, J., Qi, W., Liu, Y., Liang, H., Chaudhuri, A. R., et al. (2009) · The Journals of Gerontology Series A · doi:10.1093/gerona/glp100 · Cited by 201 · see citing works

Oxidative damage and phospholipid fatty acyl composition in skeletal muscle mitochondria from mice underexpressing or overexpressing uncoupling protein 3

BRAND, M. D., PAMPLONA, R., PORTERO-OTÍN, M., REQUENA, J. R., ROEBUCK, S. J., BUCKINGHAM, J. A., CLAPHAM, J. C., & CADENAS, S. (2002) · Biochemical Journal · doi:10.1042/bj20021077 · Cited by 184 · see citing works

Uncoupling proteins: A role in protection against reactive oxygen species—or not?

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Targeted expression of the human uncoupling protein 2 (hUCP2) to adult neurons extends life span in the fly

Fridell, Y.-W. C., Sánchez-Blanco, A., Silvia, B. A., & Helfand, S. L. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.005 · Cited by 182 · see citing works

A significant portion of mitochondrial proton leak in intact thymocytes depends on expression of UCP2

Krauss, S., Zhang, C., & Lowell, B. B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012410699 · Cited by 173 · see citing works

Long-term caloric restriction increases UCP3 content but decreases proton leak and reactive oxygen species production in rat skeletal muscle mitochondria

Bevilacqua, L., Ramsey, J. J., Hagopian, K., Weindruch, R., & Harper, M.-E. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00435.2004 · Cited by 172 · see citing works

Effects of short- and medium-term calorie restriction on muscle mitochondrial proton leak and reactive oxygen species production

Bevilacqua, L., Ramsey, J. J., Hagopian, K., Weindruch, R. H., & Harper, M. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00367.2003 · Cited by 168 · see citing works

Persistent oxidative stress due to absence of uncoupling protein 2 associated with impaired pancreatic β-cell function.

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Uncoupling Protein 2 and Islet Function

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Dinitrophenol and obesity: an early twentieth-century regulatory dilemma

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